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P34038

- KPYK_LACDE

UniProt

P34038 - KPYK_LACDE

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Protein

Pyruvate kinase

Gene
pyk
Organism
Lactobacillus delbrueckii subsp. bulgaricus
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + pyruvate = ADP + phosphoenolpyruvate.

Cofactori

Magnesium.
Potassium.

Enzyme regulationi

Strongly activated by glucose-6-phosphate, ribose-5-phosphate and fructose-6-phosphate. Weak activator AMP and weak inhibitor fructose-1,6-bisphosphate can act as strong inhibitors in the presence of strong activators.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei32 – 321Substrate By similarity
Metal bindingi34 – 341Potassium By similarity
Metal bindingi36 – 361Potassium By similarity
Metal bindingi66 – 661Potassium By similarity
Metal bindingi67 – 671Potassium; via carbonyl oxygen By similarity
Sitei221 – 2211Transition state stabilizer By similarity
Metal bindingi223 – 2231Magnesium By similarity
Binding sitei246 – 2461Substrate; via amide nitrogen By similarity
Metal bindingi247 – 2471Magnesium By similarity
Binding sitei247 – 2471Substrate; via amide nitrogen By similarity
Binding sitei279 – 2791Substrate By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. magnesium ion binding Source: InterPro
  3. potassium ion binding Source: InterPro
  4. pyruvate kinase activity Source: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium, Pyruvate

Enzyme and pathway databases

UniPathwayiUPA00109; UER00188.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate kinase (EC:2.7.1.40)
Short name:
PK
Gene namesi
Name:pyk
OrganismiLactobacillus delbrueckii subsp. bulgaricus
Taxonomic identifieri1585 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 589589Pyruvate kinasePRO_0000112076Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Structurei

3D structure databases

ProteinModelPortaliP34038.
SMRiP34038. Positions 1-589.

Family & Domainsi

Sequence similaritiesi

Belongs to the pyruvate kinase family.
In the C-terminal section; belongs to the PEP-utilizing enzyme family.

Family and domain databases

Gene3Di2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
3.50.30.10. 1 hit.
InterProiIPR008279. PEP-util_enz_mobile_dom.
IPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
IPR011037. Pyrv_Knase-like_insert_dom.
IPR015794. Pyrv_Knase_a/b.
IPR015793. Pyrv_Knase_brl.
IPR015795. Pyrv_Knase_C.
IPR015806. Pyrv_Knase_insert_dom.
[Graphical view]
PANTHERiPTHR11817. PTHR11817. 1 hit.
PfamiPF00391. PEP-utilizers. 1 hit.
PF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSiPR01050. PYRUVTKNASE.
SUPFAMiSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsiTIGR01064. pyruv_kin. 1 hit.

Sequencei

Sequence statusi: Complete.

P34038-1 [UniParc]FASTAAdd to Basket

« Hide

MKKTKIVSTL GPASDDIETI TKLAEAGANV FRFNFSHGNH EEHLARMNMV    50
REVEKKTGKL LGIALDTKGA EIRTTDQEGG KFTINTGDEI RVSMDATKAG 100
NKDMIHVTYP GLFDDTHVGG TVLIDDGAVG LTIKAKDEEK RELVCEAQNT 150
GVIGSKKGVN APGVEIRLPG ITEKDTDDIR FGLKHGINFI FASFVRKAQD 200
VLDIRALCEE ANASYVKIFP KIESQEGIDN IDEILQVSDG LMVARGDMGV 250
EIPFINVPFV QKTLIKKCNA LGKPVITATQ MLDSMQENPR PTRAEVTDVA 300
NAVLDGTDAT MLSGESANGL YPVQSVQAMH DIDVRTEKEL DTRNTLALQR 350
FEEYKGSNVT EAIGESVVRT AQELGVKTII AATSSGYTAR MISKYRPDAT 400
IVALTFDEKI QHSLGIVWGV EPVLAKKPSN TDEMFEEAAR VAKEHGFVKD 450
GDLVIIVAGV PFGQSGTTNL MKLQIIGNQL AQGLGVGTGS VIGKAVVANS 500
AEEANAKVHE GDILVAKTTD KDYMPAIKKA SGMIVEASGL TSHAAVVGVS 550
LGIPVVVGVA DATSKIADGS TLTVDARRGA IYQGEVSNL 589
Length:589
Mass (Da):62,920
Last modified:February 1, 1996 - v3
Checksum:i2BA3D3CF7AE290F1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X71403 Genomic DNA. Translation: CAA50527.1.
PIRiB48663.
S35929.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X71403 Genomic DNA. Translation: CAA50527.1 .
PIRi B48663.
S35929.

3D structure databases

ProteinModelPortali P34038.
SMRi P34038. Positions 1-589.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00188 .

Family and domain databases

Gene3Di 2.40.33.10. 1 hit.
3.20.20.60. 2 hits.
3.40.1380.20. 1 hit.
3.50.30.10. 1 hit.
InterProi IPR008279. PEP-util_enz_mobile_dom.
IPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
IPR011037. Pyrv_Knase-like_insert_dom.
IPR015794. Pyrv_Knase_a/b.
IPR015793. Pyrv_Knase_brl.
IPR015795. Pyrv_Knase_C.
IPR015806. Pyrv_Knase_insert_dom.
[Graphical view ]
PANTHERi PTHR11817. PTHR11817. 1 hit.
Pfami PF00391. PEP-utilizers. 1 hit.
PF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view ]
PRINTSi PR01050. PYRUVTKNASE.
SUPFAMi SSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
TIGRFAMsi TIGR01064. pyruv_kin. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "The genes for phosphofructokinase and pyruvate kinase of Lactobacillus delbrueckii subsp. bulgaricus constitute an operon."
    Branny P., de la Torre F., Garel J.R.
    J. Bacteriol. 178:4727-4730(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Cloning, sequencing, and expression in Escherichia coli of the gene coding for phosphofructokinase in Lactobacillus bulgaricus."
    Branny P., de la Torre F., Garel J.R.
    J. Bacteriol. 175:5344-5349(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-60.
  3. "Pyruvate kinase from Lactobacillus bulgaricus: possible regulation by competition between strong and weak effectors."
    le Bras G., Garel J.R.
    Biochimie 75:797-802(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-40, CHARACTERIZATION.

Entry informationi

Entry nameiKPYK_LACDE
AccessioniPrimary (citable) accession number: P34038
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1996
Last modified: June 11, 2014
This is version 94 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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